4L0R
Crystal structure of FGF2-interacting protein from Homo sapiens. Northeast Structural Genomics Consortium Target HR9027A.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-04-12 |
Detector | ADSC QUANTUM 4r |
Wavelength(s) | 0.979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 117.121, 70.097, 31.331 |
Unit cell angles | 90.00, 94.81, 90.00 |
Refinement procedure
Resolution | 34.040 - 2.490 |
R-factor | 0.22441 |
Rwork | 0.222 |
R-free | 0.26660 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.286 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXS |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.095 | 0.290 |
Number of reflections | 8351 | |
<I/σ(I)> | 11.1 | |
Completeness [%] | 95.9 | 79.3 |
Redundancy | 5.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microbatch under oil | 6 | 293 | 0.1 M KAcetate, 0.1 M MES, PEG 1000 40% (w/v), pH 6, Microbatch under oil, temperature 293K |